{"gene":"TG_217890","gene_symbol":"PRX1","run_date":"2026-09-10T21:09:19","timeline":{"discoveries":[{"year":2008,"finding":"TgPrx1 (typical 2-cys peroxiredoxin-1) physically interacts with the histone lysine methyltransferase KMTox, and this binding is enhanced upon oxidation, positioning TgPrx1 as a redox sensor that couples oxidative stress to epigenetic regulation of antioxidant gene expression.","method":"Co-immunoprecipitation / protein–protein interaction assay; in vitro methyltransferase activity under oxidizing and reducing conditions","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal interaction assay with functional in vitro enzyme assay, single lab","pmids":["19017266"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgPrx1 localises to the cytoplasm/nucleus (cyto-nuclear), whereas TgPrx3 localises to the mitochondrion; CRISPR-Cas9 knockout of TgPrx1 has no significant effect on in vitro infection, proliferation, or egress rates, demonstrating TgPrx1 is dispensable for the lytic cycle under standard conditions.","method":"CRISPR-Cas9 knockout confirmed by PCR, IFAT, and Western blot; immunofluorescence for localisation; in vitro growth assays","journal":"International journal of molecular sciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — CRISPR KO with multiple confirmation methods and direct localization imaging, single lab","pmids":["35328497"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":"Pru"}]},{"year":2025,"finding":"TgPRX1 is not required for the lytic cycle under standard growth conditions, but TgPRX1 knockout parasites show increased susceptibility to exogenous H2O2, confirming its role in peroxide detoxification. Combined deletion of TgPRX1 and TgPRX2 impairs parasite growth, indicating functional redundancy between these two cytosolic peroxidases.","method":"CRISPR-Cas9 single and double knockout; H2O2 susceptibility assay; in vitro growth assay","journal":"FASEB journal","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — genetic loss-of-function with orthogonal assays (lytic cycle, H2O2 challenge, double-KO epistasis) establishing functional redundancy","pmids":["40059453"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"finding":"Recombinant TgPrx1 treatment of murine macrophages triggers IL-12p40 and IL-6 production and activates NF-κB, demonstrating that TgPrx1 has immune-stimulating activity as a secreted/released antigen.","method":"Recombinant protein stimulation of murine peritoneal macrophages and RAW 264.7 cells; cytokine ELISA; NF-κB activation assay","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct biochemical stimulation assay with two orthogonal readouts (cytokine secretion and NF-κB), single lab","pmids":["28448521"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgPRX1 is a cytosolic (and partly nuclear) 2-cys peroxiredoxin that detoxifies H2O2 in a functionally redundant manner with TgPRX2, interacts with the histone methyltransferase KMTox in a redox-sensitive manner to couple oxidative stress to chromatin-level regulation of antioxidant genes, and activates macrophage NF-κB/IL-12 signalling when released from the parasite; its individual loss is dispensable for the lytic cycle under standard conditions but renders parasites hypersensitive to exogenous peroxide."},"narrative":{"mechanistic_narrative":"TgPRX1 is a typical 2-cys peroxiredoxin of Toxoplasma gondii that detoxifies hydrogen peroxide as part of the parasite's antioxidant defence network [PMID:40059453]. It localises to the cytoplasm and nucleus, and its individual deletion has no effect on the in vitro lytic cycle under standard conditions, yet renders parasites hypersensitive to exogenous H2O2; combined loss of TgPRX1 and the cytosolic peroxidase TgPRX2 impairs growth, establishing functional redundancy between the two enzymes [PMID:35328497, PMID:40059453]. Beyond peroxide scavenging, TgPRX1 physically interacts with the histone lysine methyltransferase KMTox in an oxidation-enhanced manner, positioning it as a redox sensor that links oxidative stress to chromatin-level regulation [PMID:19017266]. As a released antigen, recombinant TgPRX1 stimulates murine macrophages to produce IL-12p40 and IL-6 and activates NF-κB, giving it an additional immune-stimulating role [PMID:28448521].","teleology":[{"year":2008,"claim":"Whether peroxiredoxins do more than scavenge peroxide was addressed by showing TgPrx1 binds the histone methyltransferase KMTox with oxidation-enhanced affinity, positioning it as a redox sensor coupling oxidative stress to epigenetic regulation.","evidence":"Co-immunoprecipitation interaction assay plus in vitro methyltransferase activity under oxidizing and reducing conditions","pmids":["19017266"],"confidence":"Medium","gaps":["Downstream target genes of KMTox-coupled regulation not defined in vivo","Single lab, no genetic validation of the interaction's function","Structural basis of oxidation-enhanced binding unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"claim":"A role for TgPrx1 beyond intracellular antioxidant function was revealed when the recombinant protein stimulated macrophages, establishing it as an immune-active released antigen.","evidence":"Recombinant protein stimulation of murine macrophages and RAW 264.7 cells with cytokine ELISA and NF-κB activation assay","pmids":["28448521"],"confidence":"Medium","gaps":["Receptor mediating macrophage activation not identified","Uses recombinant protein rather than parasite-derived secreted protein","Physiological significance during infection not tested"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"The requirement of TgPRX1 for the parasite lytic cycle was tested by CRISPR knockout, which showed no effect on infection, proliferation, or egress and confirmed a cyto-nuclear localisation distinct from mitochondrial TgPrx3.","evidence":"CRISPR-Cas9 knockout confirmed by PCR, IFAT, Western blot; immunofluorescence localisation; in vitro growth assays in strain Pru","pmids":["35328497"],"confidence":"Medium","gaps":["Dispensability tested only under standard, non-stress conditions","No stress-challenge phenotype assessed here","Redundancy with other peroxiredoxins not tested"],"attribution":[{"species":"Toxoplasma gondii","strain":"Pru"}]},{"year":2025,"claim":"The functional context of TgPRX1's dispensability was resolved by showing single knockouts are hypersensitive to exogenous H2O2 and that TgPRX1/TgPRX2 double deletion impairs growth, establishing genetic redundancy between the two cytosolic peroxidases in peroxide detoxification.","evidence":"CRISPR-Cas9 single and double knockouts with H2O2 susceptibility and in vitro growth assays","pmids":["40059453"],"confidence":"High","gaps":["Molecular basis of redundancy (shared substrates/regulation) not defined","In vivo relevance during host infection not established","Relationship between peroxidase and KMTox/immune functions not integrated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["KMTOX (HISTONE LYSINE METHYLTRANSFERASE)","TGPRX2 (FUNCTIONALLY REDUNDANT CYTOSOLIC PEROXIDASE)"],"other_free_text":["TgPRX1 binding to KMTox is enhanced under oxidizing conditions, consistent with a redox-sensor function [#1].","TgPRX1 and TgPRX2 are functionally redundant; only double deletion impairs parasite growth [#3].","Recombinant TgPRX1 induces IL-12p40, IL-6 and NF-κB activation in murine macrophages, indicating immune-stimulating activity as a released antigen [#4]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"14651610","id":"PMC_14651610","title":"The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury.","date":"2004","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/14651610","citation_count":105,"is_preprint":false},{"pmid":"28448521","id":"PMC_28448521","title":"Immunization with Toxoplasma gondii peroxiredoxin 1 induces protective immunity against toxoplasmosis in mice.","date":"2017","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/28448521","citation_count":22,"is_preprint":false},{"pmid":"19017266","id":"PMC_19017266","title":"The histone methylase KMTox interacts with the redox-sensor peroxiredoxin-1 and targets genes involved in Toxoplasma gondii antioxidant defences.","date":"2008","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/19017266","citation_count":14,"is_preprint":false},{"pmid":"34816403","id":"PMC_34816403","title":"Macrophage Stimulation as a Useful Approach for Immunoscreening of Potential Vaccine Candidates Against Toxoplasma gondii and Neospora caninum Infections.","date":"2022","source":"Methods in molecular biology (Clifton, N.J.)","url":"https://pubmed.ncbi.nlm.nih.gov/34816403","citation_count":3,"is_preprint":false},{"pmid":"35328497","id":"PMC_35328497","title":"Genetic Disruption of Toxoplasma gondii peroxiredoxin (TgPrx) 1 and 3 Reveals the Essential Role of TgPrx3 in Protecting Mice from Fatal Consequences of Toxoplasmosis.","date":"2022","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/35328497","citation_count":2,"is_preprint":false},{"pmid":"40059453","id":"PMC_40059453","title":"Toxoplasma survives the loss of key enzymes of peroxide and glutathione metabolism.","date":"2025","source":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","url":"https://pubmed.ncbi.nlm.nih.gov/40059453","citation_count":1,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5545,"output_tokens":1429,"usd":0.019035,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6488,"output_tokens":2837,"usd":0.051682,"stage2_stop_reason":"end_turn"},"total_usd":0.070717,"stage1_batch_id":"msgbatch_01WokvBYTB6JLnYrpD4rXnyV","stage2_batch_id":"msgbatch_01M7hsQDvz6AqVC9DLVjQzzc","note":"batch pricing = 50% of standard","corrective_rerun":"2026-09-10 wrong-gene rerun (round-4 rules)","corrective_reason":"summary amended"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2004,\n      \"finding\": \"TgPrx2 (a cytosolic 1-cys peroxiredoxin) overexpression in T. gondii increases protection against H2O2 treatment, indicating it functions as a peroxidase contributing to the antioxidant defence network alongside catalase.\",\n      \"method\": \"Transgenic overexpression of TgPrx2 followed by H2O2 challenge assay\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean genetic manipulation with defined phenotypic readout (H2O2 resistance), single lab but orthogonal to catalase KO experiment\",\n      \"pmids\": [\"14651610\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"TgPrx1 (typical 2-cys peroxiredoxin-1) physically interacts with the histone lysine methyltransferase KMTox, and this binding is enhanced upon oxidation, positioning TgPrx1 as a redox sensor that couples oxidative stress to epigenetic regulation of antioxidant gene expression.\",\n      \"method\": \"Co-immunoprecipitation / protein–protein interaction assay; in vitro methyltransferase activity under oxidizing and reducing conditions\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal interaction assay with functional in vitro enzyme assay, single lab\",\n      \"pmids\": [\"19017266\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgPrx1 localises to the cytoplasm/nucleus (cyto-nuclear), whereas TgPrx3 localises to the mitochondrion; CRISPR-Cas9 knockout of TgPrx1 has no significant effect on in vitro infection, proliferation, or egress rates, demonstrating TgPrx1 is dispensable for the lytic cycle under standard conditions.\",\n      \"method\": \"CRISPR-Cas9 knockout confirmed by PCR, IFAT, and Western blot; immunofluorescence for localisation; in vitro growth assays\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CRISPR KO with multiple confirmation methods and direct localization imaging, single lab\",\n      \"pmids\": [\"35328497\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TgPRX1 is not required for the lytic cycle under standard growth conditions, but TgPRX1 knockout parasites show increased susceptibility to exogenous H2O2, confirming its role in peroxide detoxification. Combined deletion of TgPRX1 and TgPRX2 impairs parasite growth, indicating functional redundancy between these two cytosolic peroxidases.\",\n      \"method\": \"CRISPR-Cas9 single and double knockout; H2O2 susceptibility assay; in vitro growth assay\",\n      \"journal\": \"FASEB journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — genetic loss-of-function with orthogonal assays (lytic cycle, H2O2 challenge, double-KO epistasis) establishing functional redundancy\",\n      \"pmids\": [\"40059453\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Recombinant TgPrx1 treatment of murine macrophages triggers IL-12p40 and IL-6 production and activates NF-κB, demonstrating that TgPrx1 has immune-stimulating activity as a secreted/released antigen.\",\n      \"method\": \"Recombinant protein stimulation of murine peritoneal macrophages and RAW 264.7 cells; cytokine ELISA; NF-κB activation assay\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct biochemical stimulation assay with two orthogonal readouts (cytokine secretion and NF-κB), single lab\",\n      \"pmids\": [\"28448521\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgPRX1 is a cytosolic (and partly nuclear) 2-cys peroxiredoxin that detoxifies H2O2 in a functionally redundant manner with TgPRX2, interacts with the histone methyltransferase KMTox in a redox-sensitive manner to couple oxidative stress to chromatin-level regulation of antioxidant genes, and activates macrophage NF-κB/IL-12 signalling when released from the parasite; its individual loss is dispensable for the lytic cycle under standard conditions but renders parasites hypersensitive to exogenous peroxide.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TgPRX1 is a typical 2-cys peroxiredoxin of Toxoplasma gondii that detoxifies hydrogen peroxide as part of the parasite's antioxidant defence network [#3]. It localises to the cytoplasm and nucleus, and its individual deletion has no effect on the in vitro lytic cycle under standard conditions, yet renders parasites hypersensitive to exogenous H2O2; combined loss of TgPRX1 and the cytosolic peroxidase TgPRX2 impairs growth, establishing functional redundancy between the two enzymes [#2, #3]. Beyond peroxide scavenging, TgPRX1 physically interacts with the histone lysine methyltransferase KMTox in an oxidation-enhanced manner, positioning it as a redox sensor that links oxidative stress to chromatin-level regulation [#1]. As a released antigen, recombinant TgPRX1 stimulates murine macrophages to produce IL-12p40 and IL-6 and activates NF-\\u03baB, giving it an additional immune-stimulating role [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2004,\n      \"claim\": \"Establishing that Toxoplasma peroxiredoxins act as functional peroxidases, overexpression of the related cytosolic TgPrx2 protected parasites against H2O2, defining peroxiredoxins as contributors to the antioxidant defence network.\",\n      \"evidence\": \"Transgenic overexpression of TgPrx2 with H2O2 challenge assay in T. gondii\",\n      \"pmids\": [\"14651610\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Addresses TgPrx2, not TgPRX1 directly\", \"Overexpression rather than loss-of-function\", \"Does not establish substrate specificity or catalytic mechanism\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"Whether peroxiredoxins do more than scavenge peroxide was addressed by showing TgPrx1 binds the histone methyltransferase KMTox with oxidation-enhanced affinity, positioning it as a redox sensor coupling oxidative stress to epigenetic regulation.\",\n      \"evidence\": \"Co-immunoprecipitation interaction assay plus in vitro methyltransferase activity under oxidizing and reducing conditions\",\n      \"pmids\": [\"19017266\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Downstream target genes of KMTox-coupled regulation not defined in vivo\", \"Single lab, no genetic validation of the interaction's function\", \"Structural basis of oxidation-enhanced binding unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"A role for TgPrx1 beyond intracellular antioxidant function was revealed when the recombinant protein stimulated macrophages, establishing it as an immune-active released antigen.\",\n      \"evidence\": \"Recombinant protein stimulation of murine macrophages and RAW 264.7 cells with cytokine ELISA and NF-\\u03baB activation assay\",\n      \"pmids\": [\"28448521\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Receptor mediating macrophage activation not identified\", \"Uses recombinant protein rather than parasite-derived secreted protein\", \"Physiological significance during infection not tested\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"The requirement of TgPRX1 for the parasite lytic cycle was tested by CRISPR knockout, which showed no effect on infection, proliferation, or egress and confirmed a cyto-nuclear localisation distinct from mitochondrial TgPrx3.\",\n      \"evidence\": \"CRISPR-Cas9 knockout confirmed by PCR, IFAT, Western blot; immunofluorescence localisation; in vitro growth assays in strain Pru\",\n      \"pmids\": [\"35328497\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Dispensability tested only under standard, non-stress conditions\", \"No stress-challenge phenotype assessed here\", \"Redundancy with other peroxiredoxins not tested\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"The functional context of TgPRX1's dispensability was resolved by showing single knockouts are hypersensitive to exogenous H2O2 and that TgPRX1/TgPRX2 double deletion impairs growth, establishing genetic redundancy between the two cytosolic peroxidases in peroxide detoxification.\",\n      \"evidence\": \"CRISPR-Cas9 single and double knockouts with H2O2 susceptibility and in vitro growth assays\",\n      \"pmids\": [\"40059453\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular basis of redundancy (shared substrates/regulation) not defined\", \"In vivo relevance during host infection not established\", \"Relationship between peroxidase and KMTox/immune functions not integrated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown how TgPRX1's peroxide-detoxifying, KMTox-coupled epigenetic, and macrophage-activating activities are integrated during infection, and which downstream genes or receptors mediate these effects.\",\n      \"evidence\": \"No direct experimental evidence in the available corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No in vivo virulence or infection phenotype for TgPRX1 loss\", \"KMTox target genes and macrophage receptor unidentified\", \"No structural or catalytic mechanism characterized\"],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051920\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0004601\", \"supporting_discovery_ids\": [0, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0042744\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0006979\", \"supporting_discovery_ids\": [1, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0007249\", \"supporting_discovery_ids\": [4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"KMTox (histone lysine methyltransferase)\", \"TgPRX2 (functionally redundant cytosolic peroxidase)\"],\n    \"other_free_text\": [\n      \"TgPRX1 binding to KMTox is enhanced under oxidizing conditions, consistent with a redox-sensor function [#1].\",\n      \"TgPRX1 and TgPRX2 are functionally redundant; only double deletion impairs parasite growth [#3].\",\n      \"Recombinant TgPRX1 induces IL-12p40, IL-6 and NF-\\u03baB activation in murine macrophages, indicating immune-stimulating activity as a released antigen [#4].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_217890","name":"PRX1","product":"peroxiredoxin PRX1","uniprot_acc":"A0A125YNG8","chromosome":"TGME49_chrXII","start_pos":2203786},{"strain":"GT1","gene_id":"TGGT1_217890","name":null,"product":"putative alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen","uniprot_acc":null,"chromosome":"TGGT1_chrXII","start_pos":2143499},{"strain":"RH88","gene_id":"TGRH88_059900","name":null,"product":"putative alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen","uniprot_acc":null,"chromosome":"CM023093","start_pos":2214975},{"strain":"VEG","gene_id":"TGVEG_217890","name":null,"product":"putative alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen","uniprot_acc":"A0A0F7V741","chromosome":"TGVEG_chrXII","start_pos":2177093}]}